Patent US4278760A successfully refreshed from Google Patents.
US4278760A
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Method and composition for determining an oxidized pyridine co-enzyme
Assignee: Roche Diagnostics GmbH
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Filing: 1979-07-19
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Granted: 1981-07-14
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Expires: 1999-07-19
Abstract
Abstract A method for the quantitative determination of an oxidized pyridine co-enzyme which comprises reacting a sample containing oxidized pyridine co-enzyme in the presence of its specific alcohol dehydrogenase with an aliphatic alcohol of 8 to 16 carbon atoms, oxidizing the aldehyde formed with reduced flavine mononucleotide and oxygen in the presence of luciferase and of the particular FMN-reductase which is independent of the co-enzyme to be determined and of the reduced substrate co-enzyme of the latter, and measuring the resulting light emission as a measure of the initial oxidized pyridine co-enzyme content.
Inventors
- 👤 Karl Wulff
- 👤 Fritz Stahler
- 👤 Gerhard Michal
Bibliographic Details
Application Number
—
Jurisdiction
US
Data Source
google_patents
Last Synchronized
2026-11-02 19:45
CPC Classifications
C; C12; C12Q; C12Q1/00; C12Q1/66; C12Q1/008
Claims Analysis
Total Claims: 16
Claim 1
Independent Claim
91 words
Method for the quantitative determination of an oxidized pyridine co-enzyme which comprises reacting a sample containing oxidized pyridine co-enzyme in the presence of its specific alcohol dehydrogenase with an aliphatic alcohol of 8 to 16 carbon atoms, oxidizing the aldehyde formed with reduced flavine mononucleotide and oxygen in the presence of luciferase and of the particular FMN-reductase which is independent of the co-enzyme to be determined and of the reduced substrate co-enzyme of the latter, and measuring the resulting light emission as a measure of the initial oxidized pyrizine co-enzyme content.
Claim 2
Dependent Claim
91 words
Method for the quantitative determination of an oxidized pyridine co-enzyme which comprises reacting a sample containing oxidized pyridine co-enzyme in the presence of its specific alcohol dehydrogenase with an aliphatic alcohol of 8 to 16 carbon atoms, oxidizing the aldehyde formed with reduced flavine mononucleotide and oxygen in the presence of luciferase and of the particular FMN-reductase which is independent of the co-enzyme to be determined and of the reduced substrate co-enzyme of the latter, and measuring the resulting light emission as a measure of the initial oxidized pyrizine co-enzyme content.
Claim 3
Dependent Claim
21 words
Method as claimed in claim 1 wherein said luciferase and FMN-reductase is supplied in the form of a crude photobacteria preparation.
Claim 4
Dependent Claim
22 words
Method as claimed in claim 1 wherein the oxidized pyridine co-enzyme to be determined is simultaneously formed in a preceding dehydrogenase reaction.
Claim 5
Dependent Claim
44 words
Method as claimed in claim 3 wherein there is used purified luciferase and an FMN-reductase preparation which is independent of the oxidized pyridine co-enzyme to be determined and does not contain any FMN-reductase which is independent upon the oxidized pyridine co-enzyme to be determined.
Claim 6
Dependent Claim
10 words
Method as claimed in claim 1 wherein NAD is determined.
Claim 7
Dependent Claim
19 words
Method as claimed in claim 5 wherein said specific alcohol dehydrogenase is alcohol dehydrogenase from equine liver or yeast.
Claim 8
Dependent Claim
20 words
Method as claimed in claim 5 wherein there is used as said specific alcohol dehydrogenase, alcohol dehydrogenase from Leuconostoc mesenteroides.
Claim 9
Dependent Claim
40 words
Reagent for the determination of an oxidized pyridine co-enzyme comprising luciferase; FMN reductase; an aliphatic alcohol of 8 to 16 carbon atoms; a reduced co-enzyme; an alcohol dehydrogenase specific for the co-enzyme to be determined; flavine-mononucleotide (FMN); and a buffer.
Claim 10
Dependent Claim
40 words
Reagent for the determination of an oxidized pyridine co-enzyme comprising luciferase; FMN reductase; an aliphatic alcohol of 8 to 16 carbon atoms; a reduced co-enzyme; an alcohol dehydrogenase specific for the co-enzyme to be determined; flavine-mononucleotide (FMN); and a buffer.
Claim 11
Dependent Claim
12 words
Reagent as claimed in claim 8 also containing an organic sulphhydryl compound.
Claim 12
Dependent Claim
11 words
Reagent as claimed in claim 8 also containing a surface-active agent.
Claim 13
Dependent Claim
55 words
Reagent as claimed in claim 8 comprising 0.5 to 50 μg/ml luciferase/FMN-reductase preparation; 0.5 to 300 mU/ml alcohol dehydrogenase; 0.01 to 25 mMol/l aliphatic alcohol of 8 to 16 carbon atoms; 2to 130 mMol/l buffer, pH 6 to 9; 1 to 250×10 -6 Mol/l reduced co-enzyme; and, optionally, 0.002 to 0.5 mMol/l organic sulphhydryl compound.
Claim 14
Dependent Claim
46 words
Reagent as claimed in claim 8 comrising 1.8 to 40 μg/ml luciferase/FMN-reductase preparation; 1.3 to 2.7 mU/ml alcohol dehydrogenase; 0.1 to 10 mMol/l alcohol; 5 to 50 mMol/l buffer; 5 to 150×10 -6 Mol/l reduced pyridine co-enzyme; and, optionally, 0.005 to 0.5 mMol/l organic sulphyhydryl compound.
Claim 15
Dependent Claim
12 words
Reagent as claimed in claim 8 wherein the sulphyhydryl compound is mercaptoethanol.
Claim 16
Dependent Claim
19 words
Reagent as claimed in claim 8 wherein said reagent contains an aralkyl-polyoxyethylene ester or ether as a surface-active agent.
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USPTO Annuity & Maintenance Windows
| Annuity Stage | Window Opens | Payment Deadline | Surcharge Period Until | Estimated Fee | Status |
|---|---|---|---|---|---|
| 3.5 Years (Year 4) | 1984-07-13 | 1985-01-12 | 1985-07-14 | $2000.00 | Window Closed / Lapsed |
| 7.5 Years (Year 8) | 1988-07-13 | 1989-01-12 | 1989-07-14 | $3760.00 | Window Closed / Lapsed |
| 11.5 Years (Year 12) | 1992-07-13 | 1993-01-12 | 1993-07-14 | $7700.00 | Window Closed / Lapsed |